Dinda N

EC 1.1.1.
26
Accepted name: glyoxylate reductase
Reaction: glycolate + NAD+ = glyoxylate + NADH + H+
Other name(s): NADH-glyoxylate reductase; glyoxylic acid reductase; NADHdependent glyoxylate reductase
Systematic name: glycolate:NAD+ oxidoreductase
Comments: Reduces glyoxylate to glycolate or hydroxypyruvate to D-glycerate.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, vMetacyc, PDB,
CAS registry number: 9028-32-4
References:
1. Zelitch, I. Oxidation and reduction of glycolic and glyoxylic acids in plants. II.
Glyoxylic acid reductase. J. Biol. Chem. 201 (1953) 719-726.
2. Zelitch, I. The isolation and action of crystalline glyoxylic acid reductase from
tobacco leaves. J. Biol. Chem. 216 (1955) 553-575.
EC 1.1.1.3
Accepted name: homoserine dehydrogenase
Reaction: L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H +
H+
For diagram click here.
Other name(s): HSDH; HSD
Systematic name: L-homoserine:NAD(P)+ oxidoreductase
Comments: The yeast enzyme acts most rapidly with NAD+;
the Neurospora enzyme with NADP+. The enzyme from Escherichia coli is a
multi-functional protein, which also catalyses the reaction of EC 2.7.2.4 (aspartate
kinase).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB,

References:
1. Black, S. and Wright, N.G. Homoserine dehydrogenase. J. Biol. Chem. 213
(1955) 51-60.
2. Starnes, W.L., Munk, P., Maul, S.B., Cunningham, G.N., Cox, D.J. and Shive,
W. Threonine-sensitive aspartokinase-homoserine dehydrogenase complex, amino
acid composition, molecular weight, and subunit composition of the
complex. Biochemistry 11 (1972) 677-687. [PMID: 4551091]
3. Vron, M., Falcoz-Kelly, F. and Cohen, G.N. The threonine-sensitive
homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12.
The two catalytic activities are carried by two independent regions of the
polypeptide chain. Eur. J. Biochem. 28 (1972) 520-527. [PMID: 4562990]
EC 2.1.1.147
Accepted name: corydaline synthase
Reaction: S-adenosyl-L-methionine + palmatine + 2 NADPH + H+ = S-adenosyl-Lhomocysteine + corydaline + 2 NADP+
For diagram click here.
Systematic name: S-adenosyl-L-methionine:protoberberine 13-C-methyltransferase
Comments: Also acts on 7,8-dihydropalmatine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
155807-67-3
References:
1. Rueffer, M., Bauer, W. and Zenk, M.H. The formation of corydaline and related alkaloids
in Corydalis cava in vivo and in vitro. Canad. J. Chem. 72 (1994) 170-175.
[EC 2.1.1.147 created 2002]
EC 2.1.1.148
Accepted name: thymidylate synthase (FAD)
Reaction: 5,10-methylenetetrahydrofolate + dUMP + NADPH + H+ = dTMP +
tetrahydrofolate + NADP+
For diagram of reaction click here.
Other name(s): Thy1; ThyX
Systematic name: 5,10-methylenetetrahydrofolate,FADH2:dUMP C-methyltransferase
Comments: Contains FAD. All thymidylate synthases catalyse a reductive methylation
involving the transfer of the methylene group of 5,10-methylenetetrahydrofolate to the C5position of dUMP and a two electron reduction of the methylene group to a methyl group.
Unlike the classical thymidylate synthase, ThyA (EC 2.1.1.45), which uses folate as both a 1carbon donor and a source of reducing equivalents, this enzyme uses a flavin coenzyme as a
source of reducing equivalents, which are derived from NADPH.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry
number: 850167-13-4
References:
1. Myllykallio, H., Lipowski, G., Leduc, D., Filee, J., Forterre, P. and Liebl, U. An alternative
flavin-dependent mechanism for thymidylate synthesis. Science 297 (2002) 105-107.
[PMID: 12029065]
2. Griffin, J., Roshick, C., Iliffe-Lee, E. and McClarty, G. Catalytic mechanism of Chlamydia
trachomatis flavin-dependent thymidylate synthase. J. Biol. Chem. 280 (2005) 5456-5467.
[PMID: 15591067]
3. Graziani, S., Bernauer, J., Skouloubris, S., Graille, M., Zhou, C.Z., Marchand, C.,
Decottignies, P., van Tilbeurgh, H., Myllykallio, H. and Liebl, U. Catalytic mechanism and
structure of viral flavin-dependent thymidylate synthase ThyX. J. Biol. Chem. 281 (2006)
24048-24057. [PMID: 16707489]
4. Koehn, E.M., Fleischmann, T., Conrad, J.A., Palfey, B.A., Lesley, S.A., Mathews, I.I. and
Kohen, A. An unusual mechanism of thymidylate biosynthesis in organisms containing
the thyX gene. Nature 458 (2009) 919-923. [PMID: 19370033]
5. Koehn, E.M. and Kohen, A. Flavin-dependent thymidylate synthase: a novel pathway
towards thymine. Arch. Biochem. Biophys. 493 (2010) 96-102. [PMID: 19643076]
[EC 2.1.1.148 created 2003, modified 2010]
[EC 2.1.1.149 Deleted entry: myricetin O-methyltransferase. Now covered by EC 2.1.1.267,

flavonoid 3',5'-methyltransferase. (EC 2.1.1.149 created 2003, modified 2011, deleted 2013)]
EC 2.-.-.- Transferases. [21,296 PDB entries]

EC 2.1.-.- Transferring one-carbon groups.
[1,967 PDB entries]
1kq4
EC 2.1.1.- Methyltransferases. [1,624 PDB

entries]
EC 2.1.1.148 Thymidylate synthase

(FAD). [40 PDB entries]
Reacti 5,10-methylenetetrahydrofolate + dUMP + Nadph = dTMP + tetrahydrofolate +
on: NADP(+).
+
5,10methylenete
dUMP
trahydrofol
ate
=
NADPH
+
dTMP
+
tetrahydrof
olate
NADP(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.
Other Fdts. Flavin dependent thymidylate synthase.
name(
s):
Com Contains Fad. All thymidylate synthases catalyze a reductive methylation involving
ments the transfer of the methylene group of 5,10-methylenetetrahydrofolate to the C5: position of dUMP and a two electron reduction of the methylene group to a methyl
group. Unlike the classical thymidylate synthase, ThyA (EC 2.1.1.45), which uses
folate as both a 1-carbon donor and a source of reducing equivalents, this enzyme
uses a flavin coenzyme as a source of reducing equivalents, which are derived from
Nadph.
Links:
[IntEnz] [ExPASy] [KEGG]
There are 40 PDB entries in enzyme class E.C.2.1.1.148
EC 3.1.1.8
Accepted name: cholinesterase
Reaction: An acylcholine + H2O = choline + a carboxylate
Other name(s): pseudocholinesterase; butyrylcholine esterase; non-specific
cholinesterase; choline esterase II (unspecific); benzoylcholinesterase; choline
esterase; butyrylcholinesterase; propionylcholinesterase; BtChoEase
Systematic name: acylcholine acylhydrolase
Comments: Acts on a variety of choline esters and a few other compounds.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS
registry number: 9001-08-5
References:
1. Augustinsson, K.-B. Cholinesterases. A study in comparative enzymology. Acta
Physiol. Scand. 15, Suppl. 52 (1948).
2. Augustinsson, K.-B. and Olsson, B. Esterases in the milk and blood of swine. I.
Substrate specificity and electrophoresis studies. Biochem. J. 71 (1959) 477-484.
3. Koelle, G.B. Cholinesterases of the tissues and sera of rabbits. Biochem. J. 53
(1953) 217-226.
4. Nachmansohn, D. and Wilson, I.B. The enzymic hydrolysis and synthesis of
acetylcholine. Adv. Enzymol. Relat. Subj. Biochem. 12 (1951) 259-339.
5. Sawyer, C.H. Hydrolysis of choline esters by liver. Science 101 (1945) 385-386.
6. Strelitz, F. Studies on cholinesterase. 4. Purification of pseudo-cholinesterase
from horse serum. Biochem. J. 38 (1944) 86-88.
[EC 3.1.1.8 created 1961]
[EC 3.1.1.9 Deleted entry: benzoylcholinesterase; a side reaction of EC

3.1.1.8 cholinesterase (EC 3.1.1.9 created 1961, deleted 1972)]
EC 3.1.1.10
Accepted name: tropinesterase
Reaction: atropine + H2O = tropine + tropate
Other name(s): tropine esterase; atropinase; atropine esterase;
Systematic name: atropine acylhydrolase
Comments: Also acts on cocaine and other tropine esters.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD,
References:
1. Glick, D., Glaubach, S. and Moore, D.H. Azolesterase activities of
electrophoretically separated proteins of serum. J. Biol. Chem. 144 (1942) 525528.
2. Moog, P. and Krisch, K. [The purification and characterization of atropine
esterase from rabbit liver microsomes]. Hoppe-Seyler's Z. Physiol. Chem. 355
(1974) 529-542. [PMID: 4435736]
EC 4.1.1.14
Accepted name: valine decarboxylase
Reaction: L-valine = 2-methylpropanamine + CO2
Other name(s): leucine decarboxylase
Systematic name: L-valine carboxy-lyase
Comments: A pyridoxal-phosphate protein. Also acts on L-leucine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD,
References:
1. Sutton, C.R. and King, H.K. Inhibition of leucine decarboxylase by thiolbinding reagents. Arch. Biochem. Biophys. 96 (1962) 360-370.
[EC 4.1.1.14 created 1961]
EC 4.1.1.15
Accepted name: glutamate decarboxylase
Reaction: L-glutamate = 4-aminobutanoate + CO2
Glossary: 4-aminobutanoate = -aminobutyrate = GABA
Other name(s): L-glutamic acid decarboxylase; L-glutamic decarboxylase; cysteic

acid decarboxylase; L-glutamate -decarboxylase; aspartate 1-decarboxylase;
aspartic -decarboxylase; L-aspartate--decarboxylase; -glutamate decarboxylase
Systematic name: L-glutamate 1-carboxy-lyase
Comments: A pyridoxal-phosphate protein. The brain enzyme also acts on Lcysteate, 3-sulfino-L-alanine and L-aspartate.
References:
1. Ambe, L. and Sohonie, K. Purification and properties of glutamate
decarboxylase from the field bean (Dolichos lablab). Enzymologia 26 (1963) 98107.
2. Nakano, Y. and Kitaoka, S. L-Aspartate -decarboxylase in a cell-free system
from Escherichia coli. J. Biochem. (Tokyo) 70 (1971) 327. [PMID: 4937550]
3. Roberts, E. and Frankel, S. Further studies of glutamic acid decarboxylase in
brain. J. Biol. Chem. 190 (1951) 505-512.
EC 5.1.1.1
Accepted name: alanine racemase
Reaction: L-alanine = D-alanine
Other name(s): L-alanine racemase
Systematic name: alanine racemase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB,
References:
1. Marr, A.G. and Wilson, P.W. The alanine racemase of Brucella abortus. Arch.
Biochem. Biophys. 49 (1954) 424-433.
2. Wood, W.A. Amino acid racemases. Methods Enzymol. 2 (1955) 212-217.
3. Wood, W.A. and Gunsalus, I.C. D-Alanine formation: a racemase
in Streptococcus faecalis. J. Biol. Chem. 190 (1951) 403-416.
[EC 5.1.1.1 created 1961]
EC 5.1.1.2
Accepted name: methionine racemase
Reaction: L-methionine = D-methionine
Systematic name: methionine racemase
Comments: A pyridoxal-phosphate protein.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry
number: 9024-07-1
References:
1. Kallio, R.E. and Larson, A.D. Methionine degradation by a species
of Pseudomonas, in McElroy, W.D. and Glass, H.B. (Eds.), A Symposium on
Amino Acid Metabolism, Johns Hopkins Press, Baltimore, 1955, pp. 616-634.
EC 6.1.1.14
Accepted name: glycinetRNA ligase
Reaction: ATP + glycine + tRNAGly = AMP + diphosphate + glycyl-tRNAGly
Other name(s): glycyl-tRNA synthetase; glycyl-transfer ribonucleate synthetase;
glycyl-transfer RNA synthetase; glycyl-transfer ribonucleic acid synthetase; glycyl
translase
Systematic name: glycine:tRNAGly ligase (AMP-forming)
References:
1. Fraser, M.J. Glycyl-RNA synthetase of rat liver: partial purification and effects
of some metal ions on its activity. Can. J. Biochem. Physiol. 41 (1963) 1123-1233.
2. Niyomporn, B., Dahl, J.L. and Strominger, J.L. Biosynthesis of the
peptidoglycan of bacterial cell walls. IX. Purification and properties of glycyl
transfer ribonucleic acid synthetase from Staphylococcus aureus. J. Biol.
Chem. 243 (1968) 773-778. [PMID: 4295604]
[EC 6.1.1.14 created 1972]
EC 6.1.1.15
Accepted name: prolinetRNA ligase
Reaction: ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro
Other name(s): prolyl-tRNA synthetase; prolyl-transferRNA synthetase; prolyltransfer ribonucleate synthetase; proline translase; prolyl-transfer ribonucleic acid
synthetase; prolyl-s-RNA synthetase; prolinyl-tRNA ligase
Systematic name: L-proline:tRNAPro ligase (AMP-forming)
References:
1. Norton, S.J. Purification and properties of the prolyl RNA synthetase
of Escherichia coli. Arch. Biochem. Biophys. 106 (1964) 147-152.
2. Peterson, P.J. and Fowden, L. Purification, properties and comparative
specificities of the enzyme prolyl-transfer ribonucleic acid synthetase
from Phaseolus aureus and Polygonatum multiflorum. Biochem. J. 97 (1965) 112124.
EC 6.-.-.- Ligases. [1,841 PDB entries]

EC 6.1.-.- Forming carbon-oxygen bonds.
[644 PDB entries]
1d2d
EC 6.1.1.- Ligases forming aminoacyl-tRNA

and related compounds. [633 PDB entries]
EC 6.1.1.15 Proline--tRNA ligase. [30 PDB

entries]
Reaction Atp + L-proline + tRNA(Pro) = amp + diphosphate + L-prolyl-tRNA(Pro).
:
+
ATP
+
Lprolin
e
AMP
tRNA(Pro
+
diphosp
hate
L-
prolyltRNA(
Pro)
Molecule diagrams generated from .mol files obtained from the KEGG ftp
site.
Other na Proline translase. Prolyl-tRNA synthetase.
me(s):
Links:
[IntEnz] [ExPASy] [KEGG]
There are 30 PDB entries in enzyme class E.C.6.1.1.15
PDB code Protein

1d2d
1fyj
1h4q
1h4s
1h4t
Hamster eprs second repeated element. Nmr, 5 structures

Source: Cricetulus griseus. Chinese hamster. Organism_taxid:
10029. Organ: ovary cells. Expressed in: escherichia coli.
Expression_system_taxid: 562.
Chain: A (56 residues) CATH domain: 1.10.287.10
Solution structure of multi-functional peptide motif-1 present in human
glutamyl-prolyl tRNA synthetase (eprs).
Source: Homo sapiens. Human. Organism_taxid: 9606.
Expressed in: escherichia coli. Expression_system_taxid: 562.
Prolyl-tRNA synthetase from thermus thermophilus complexed with
trnapro(cgg), atp and prolinol
Source: Thermus thermophilus. Organism_taxid: 274. Strain: hb8. Other_details: purification of protein described in reference 2.
Other_details: purification of trnapro described in reference 3
Chains: A, B (465 residues) CATH
domains: 3.30.930.10 3.40.50.800 3.30.110.30
Bound
Het Group ATP corresponds to enzyme reactant
ligands:
ATP
Het Group PRI is 87.00% similar to enzyme
reactant L-proline
Prolyl-tRNA synthetase from thermus thermophilus complexed with
trnapro(cgg) and a prolyl-adenylate analogue
Source: Thermus thermophilus. Organism_taxid: 274. Strain: hb8. Other_details: purification of protein described in reference 2.
Other_details: purification of trnapro described in reference 3
domains: 3.30.930.10 3.40.50.800 3.30.110.30
Bound
Het Group PSD is 70.00% similar to enzyme
ligand:
product AMP
Prolyl-tRNA synthetase from thermus thermophilus complexed with l-
1hc7
1nj1
1nj2
1nj5
1nj6
proline
Source: Thermus thermophilus. Organism_taxid: 274. Strain: hb8. Other_details: purification described in reference 2
Chains: A, B, C, D (464 residues) CATH
domains: 3.30.930.10 3.40.50.800 3.30.110.30
Bound
Het Group PRO corresponds to enzyme reactant
ligand:
L-proline
Prolyl-tRNA synthetase from thermus thermophilus
Source: Thermus thermophilus. Organism_taxid: 274. Strain: hb8. Gene: pros. Other_details: purification described in reference 2
domains: 3.30.930.10 3.40.50.800 3.30.110.30
Crystal structure of prolyl-tRNA synthetase from methanother
thermautotrophicus bound to cysteine sulfamoyl adenylate
Source: Methanothermobacter thermautotrophicus
organism_taxid: 145262. Gene: mth611. Expressed in:
escherichia coli. Expression_system_taxid: 562. Other_details:
strain supplemented with additional plasmid rare trnas
Chain: A (463 residues) CATH
domains: 3.30.930.10 3.40.50.800 3.30.110.30
Bound
Het Group 5CA is 57.58% similar to enzyme
ligand:
product AMP
thermautotrophicus
organism_taxid: 187420. Strain: delta h. Gene: mth611.
Other_details: strain supplemented with additional plasmid rare
trnas
domains: 3.30.930.10 3.40.50.800 3.30.110.30
thermautotrophicus bound to proline sulfamoyl adenylate
trnas
domains: 3.30.930.10 3.40.50.800 3.30.110.30
Bound
Het Group P5A is 55.88% similar to enzyme
ligand:
product AMP
thermautotrophicus bound to alanine sulfamoyl adenylate
trnas
1nj8
1r1b
2i4l
2i4m
2i4n
2i4o
2j3l
domains: 3.30.930.10 3.40.50.800 3.30.110.30

Bound
Het Group A5A is 59.38% similar to enzyme
ligand:
product AMP
Crystal structure of prolyl-tRNA synthetase from methanocaldococcus
janaschii
Source: Methanocaldococcus jannaschii. Organism_taxid: 2190.
Gene: mj1238. Expressed in: escherichia coli.
Expression_system_taxid: 562. Other_details: strain
supplemented with additional plasmid encoding rare trnas
domains: 3.30.930.10 3.40.50.800 3.30.110.30
Eprs second repeated element, nmr, minimized average structure
Source: Cricetulus griseus. Chinese hamster. Organism_taxid:
10029. Organ: ovary cells. Expressed in: escherichia coli.
Expression_system_taxid: 562
Rhodopseudomonas palustris prolyl-tRNA synthetase
Source: Rhodopseudomonas palustris. Organism_taxid: 1076.
Strain: cga009-atcc baa-98. Gene: pros,rpa2928. Expressed in:
escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C (439 residues) CATH
domains: 3.30.930.10 3.40.50.800
Rhodopseudomonas palustris prolyl-tRNA synthetase in complex
proams
domains: 3.30.930.10 3.40.50.800
Bound
Het Group PSD is 70.97% similar to enzyme
ligand:
product AMP
cysams
domains: 3.30.930.10 3.40.50.800
Bound
Het Group 5CA is 57.58% similar to enzyme
ligand:
product AMP
domains: 3.30.930.10 3.40.50.800
Bound ligand: Het Group ATP corresponds to enzyme reactant
ATP
Prolyl-tRNA synthetase from enterococcus faecalis complexed with a
prolyl-adenylate analogue ('5'-o-(n-(l-prolyl)- sulfamoyl)adenosine)
2j3m
3ial
4hvc
4k86
4k87
Source: Enterococcus faecalis. Organism_taxid: 1351.

domains: 3.40.50.800 3.30.930.10 3.90.960.10
Bound
Het Group P5A is 55.88% similar to enzyme
ligand:
product AMP
Prolyl-tRNA synthetase from enterococcus faecalis complexed with
atp, manganese and prolinol
Source: Enterococcus faecalis. Organism_taxid: 1351.
domains: 3.40.50.800 3.30.930.10 3.90.960.10
Bound
Het Group ATP corresponds to enzyme reactant
ligands:
ATP
Het Group PRI is 87.00% similar to enzyme
reactant L-proline
Giardia lamblia prolyl-tRNA synthetase in complex with proly
adenylate
Source: Giardia lamblia atcc 50803. Organism_taxid: 184922.
Gene: gl50803_15983, prors. Expressed in: escherichia coli.
domains: 3.30.930.10 3.40.50.800 3.30.110.30
Bound
Het Group GOL is 40.00% similar to enzyme
ligands:
reactant L-proline
Het Group PR8 is 76.67% similar to enzyme
product AMP
Crystal structure of human prolyl-tRNA synthetase in complex
halofuginone and atp analogue
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene:
eprs, glns, pars, qars, qprs, pig32. Expressed in: escherichia coli.
domains: 3.30.930.10 3.40.50.800 3.30.110.30
Crystal structure of human prolyl-tRNA synthetase (apo form)
eprs. Expressed in: escherichia coli. Expression_system_taxid:
562.
domains: 3.30.930.10 3.40.50.800 3.30.110.30
Crystal structure of human prolyl-tRNA synthetase (substrate form)
562.
domains: 3.30.930.10 3.40.50.800 3.30.110.30
Bound
Het Group PRO corresponds to enzyme reactant
ligands:
L-proline
Het Group ADN is 82.61% similar to enzyme
product AMP
4k88
4ncx
4olf
4twa
4wi1
4ydq
5a34
Crystal structure of human prolyl-tRNA synthetase (halofugin form)

562.
domains: 3.30.930.10 3.40.50.800 3.30.110.30
Crystal structure of prolyl-tRNA synthetase (prors, proline- ligase)
from plasmodium falciparum 3d7
Source: Plasmodium falciparum 3d7. Organism_taxid: 36329.
Strain: 3d7. Gene: prors, pfl0670c. Expressed in: escherichia coli.
Chains: A, B (449 residues)
Crystal structure of prolyl-tRNA synthetase (prors, proline- ligase)from
plasmodium falciparum in complex with halofugin amppnp
Source: Plasmodium falciparum. Organism_taxid: 36329. Gene:
prors, pfl0670c. Expressed in: escherichia coli.
Chain: A (482 residues)
Bound
Het Group ANP is 74.19% similar to enzyme
ligand:
product AMP
Crystal structure of prolyl-tRNA synthetase (prs) from plasm
falciparum
Source: Plasmodium falciparum. Organism_taxid: 36329. Strain:
isolate 3d7. Gene: prors, pfl0670c. Expressed in: escherichia coli.
domains: 3.30.930.10 3.40.50.800 3.30.110.30
Crystal structure of prolyl-tRNA synthetase (prors, proline- ligase)
from plasmodium falciparum in complex with tcmdc-12
Bound
Het Group IMD is 44.44% similar to enzyme
ligand:
reactant L-proline
Crystal structure of prolyl-tRNA synthetase (prs) from plasm
falciparum in complex with halofuginone and amppnp
Bound
Het Group ANP is 74.19% similar to enzyme
ligand:
product AMP
The crystal structure of the gst-like domains complex of epr
Source: Homo sapiens. Human. Organism_taxid: 9606.
Expressed in: escherichia coli. Expression_system_taxid:
469008.
Chains: A, C, E, G (168 residues)
Bound
Het Group GOL is 40.00% similar to enzyme
ligand:
reactant L-proline
5bmu
The crystal structure of the gst-like domains complex of aim mutant

c92sc105sc123s
eef1e1, aimp3, p18. Expressed in: escherichia coli.
Expression_system_taxid: 562. Gene: eprs.
Chains: B, D, F, H (166 residues)

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EC 1.1.1.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB,

[EC 2.1.1.149 Deleted entry: myricetin O-methyltransferase. Now covered by EC 2.1.1.267,

EC 2.-.-.- Transferases. [21,296 PDB entries]

EC 2.1.1.- Methyltransferases. [1,624 PDB

EC 2.1.1.148 Thymidylate synthase

[IntEnz] [ExPASy] [KEGG]

There are 40 PDB entries in enzyme class E.C.2.1.1.148

[EC 3.1.1.9 Deleted entry: benzoylcholinesterase; a side reaction of EC

Other name(s): L-glutamic acid decarboxylase; L-glutamic decarboxylase; cysteic

Comments: A pyridoxal-phosphate protein.

EC 6.-.-.- Ligases. [1,841 PDB entries]

EC 6.1.1.- Ligases forming aminoacyl-tRNA

EC 6.1.1.15 Proline--tRNA ligase. [30 PDB

[IntEnz] [ExPASy] [KEGG]

There are 30 PDB entries in enzyme class E.C.6.1.1.15

PDB code Protein

Hamster eprs second repeated element. Nmr, 5 structures

domains: 3.30.930.10 3.40.50.800 3.30.110.30

Source: Enterococcus faecalis. Organism_taxid: 1351.

Crystal structure of human prolyl-tRNA synthetase (halofugin form)

The crystal structure of the gst-like domains complex of aim mutant

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